ID   HIS82_RALSO             Reviewed;         374 AA.
AC   Q8Y0Y8;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Histidinol-phosphate aminotransferase 2;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase 2;
GN   Name=hisC2; OrderedLocusNames=RSc0905; ORFNames=RS04510;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-
CC         oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766,
CC         ChEBI:CHEBI:57980; EC=2.6.1.9;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AL646052; CAD14607.1; -; Genomic_DNA.
DR   RefSeq; WP_011000857.1; NC_003295.1.
DR   AlphaFoldDB; Q8Y0Y8; -.
DR   SMR; Q8Y0Y8; -.
DR   STRING; 267608.RSc0905; -.
DR   EnsemblBacteria; CAD14607; CAD14607; RSc0905.
DR   GeneID; 60500416; -.
DR   KEGG; rso:RSc0905; -.
DR   PATRIC; fig|267608.8.peg.927; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_4; -.
DR   OMA; NYHVAGF; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000001436; Chromosome.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR005861; HisP_aminotrans.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01141; hisC; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..374
FT                   /note="Histidinol-phosphate aminotransferase 2"
FT                   /id="PRO_0000153431"
FT   MOD_RES         227
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   374 AA;  39627 MW;  C2511E205582F030 CRC64;
     MSLQFGPEYV RAIAPYVTGK PISEVAREFG LEAARIVKLA SNENPLGMPA SARVAMTAAI
     DGLARYPDAN GFSLKAALHA KFGVPEAWIT LGNGSNDILE LAARALVAPG QGVIYAQHAF
     AVYALAAQEV GARAVEVPAR DYGHDLDAMA AAITPDTRLI YVANPNNPTG TFLPADAVAA
     FLAKVPPTVV VVLDEAYNEF LKPEQQYDSI AWVRRYPNLL VSRTFSKAYG LAGLRVGYGI
     AQPQLTALLN RIRQPFNVNS LAQAAAVAAL SDTEFLRRSA ELNAAGYAQL TQAFARLGLE
     YVPSSGNFVL VRVGDDADAG ARVNLALLRQ GVIVRPVGNY GLPQWLRISI GLPEENAACI
     AALESALAQA EAAA